Selection of m. tuberculosis clinically isolated sensitive & resistant to fluoroquinolones
Keywords:SDR, PsPA, OFX, MIC, EF-Tu, EF-P, E. Coli
In the present study we observed on performing docking analysis that OFX interacted with conserved residues of Usp, SDR, PspA and CoA transferease domain of Rv2140c, Rv0148, Rv2744c and Rv3551, respectively, which might alter this function. It is predicted that these proteins might be exhibiting increased intensities to inhibit/modulate/compensate the effect of drugs. Further, detailed study in this direction might help to search new targets for drug development. Besides known proteins, upregulation of hypothetical proteins strengthen the possibility of some unknown underlying mechanism responsible for resistance to OFX. This could be crucial for the initial survival of the cells before gene level changes could come into play to ensure survival under prolonged adverse conditions. These findings may be further exploited to develop newer therapeutic agents derived from OFX. Further detailed and in-depth investigations to explore these leads will give an insight into probable sites of drug action, other than established primary sites and hence may help in the search of novel chemotherapeutic agents at these new sites as inhibitors and could provide the mankind with some ultimate treatmentstrategies.
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